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SR34B_ARATH
ID   SR34B_ARATH             Reviewed;         278 AA.
AC   F4JHI7; C0Z3A4; O81290; Q8GXS0;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Serine/arginine-rich splicing factor SR34B;
DE            Short=At-SR34B;
DE            Short=At-SRp34B;
DE            Short=AtSR34B;
DE   AltName: Full=SER/ARG-rich protein 34B;
GN   Name=SR34B; Synonyms=SRP34B; OrderedLocusNames=At4g02430;
GN   ORFNames=T14P8.21;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   ALTERNATIVE SPLICING, AND INDUCTION.
RX   PubMed=17319848; DOI=10.1111/j.1365-313x.2006.03020.x;
RA   Palusa S.G., Ali G.S., Reddy A.S.;
RT   "Alternative splicing of pre-mRNAs of Arabidopsis serine/arginine-rich
RT   proteins: regulation by hormones and stresses.";
RL   Plant J. 49:1091-1107(2007).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=21935421; DOI=10.1371/journal.pone.0024542;
RA   Richardson D.N., Rogers M.F., Labadorf A., Ben-Hur A., Guo H.,
RA   Paterson A.H., Reddy A.S.N.;
RT   "Comparative analysis of serine/arginine-rich proteins across 27
RT   eukaryotes: insights into sub-family classification and extent of
RT   alternative splicing.";
RL   PLoS ONE 6:E24542-E24542(2011).
CC   -!- FUNCTION: Probably involved in intron recognition and spliceosome
CC       assembly.
CC   -!- SUBUNIT: Component of the spliceosome.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:O22315}.
CC       Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O22315}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=F4JHI7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4JHI7-2; Sequence=VSP_054992;
CC       Name=3;
CC         IsoId=F4JHI7-3; Sequence=VSP_054991, VSP_054992;
CC   -!- MISCELLANEOUS: The splicing pattern of the pre-mRNA is regulated in a
CC       tissue-specific manner and by development, and changes in response to
CC       various types of abiotic stresses. {ECO:0000305|PubMed:17319848}.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. SR subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC19288.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80736.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF069298; AAC19288.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161494; CAB80736.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82171.1; -; Genomic_DNA.
DR   EMBL; AK118074; BAC42705.1; -; mRNA.
DR   EMBL; AK319068; BAH57183.1; -; mRNA.
DR   PIR; T01307; T01307.
DR   RefSeq; NP_849537.1; NM_179206.3. [F4JHI7-2]
DR   AlphaFoldDB; F4JHI7; -.
DR   SMR; F4JHI7; -.
DR   BioGRID; 13318; 3.
DR   STRING; 3702.AT4G02430.2; -.
DR   PaxDb; F4JHI7; -.
DR   PRIDE; F4JHI7; -.
DR   EnsemblPlants; AT4G02430.1; AT4G02430.1; AT4G02430. [F4JHI7-2]
DR   EnsemblPlants; AT4G02430.3; AT4G02430.3; AT4G02430.
DR   GeneID; 828027; -.
DR   Gramene; AT4G02430.1; AT4G02430.1; AT4G02430. [F4JHI7-2]
DR   Gramene; AT4G02430.3; AT4G02430.3; AT4G02430.
DR   KEGG; ath:AT4G02430; -.
DR   Araport; AT4G02430; -.
DR   TAIR; locus:2133249; AT4G02430.
DR   eggNOG; KOG0105; Eukaryota.
DR   HOGENOM; CLU_012062_34_0_1; -.
DR   InParanoid; F4JHI7; -.
DR   PhylomeDB; F4JHI7; -.
DR   PRO; PR:F4JHI7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JHI7; baseline and differential.
DR   Genevisible; F4JHI7; AT.
DR   GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spliceosome.
FT   CHAIN           1..278
FT                   /note="Serine/arginine-rich splicing factor SR34B"
FT                   /id="PRO_0000429597"
FT   DOMAIN          7..82
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          120..195
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          81..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..239
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P92964"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P92964"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P92964"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VYA5"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P92966"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SJA6"
FT   MOD_RES         250
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VYA5"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FYB7"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P92966"
FT   VAR_SEQ         1..28
FT                   /note="MSSRSSRTIYVGNLPGDIREREVEDLFS -> MHLRNCWILILFGRSFLKNC
FT                   SSLFFL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_054991"
FT   VAR_SEQ         174..278
FT                   /note="LDDTEFRNAFSHEYVRVREYDSRRDSRSPSRGRSYSKSRSRGRSPSRSRSRS
FT                   RSRSKSRSPKAKSLRRSPAKSTSRSPRSRSRSKSRSLSPRGWVTVERHWIALI -> IK
FT                   KAR (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11910074,
FT                   ECO:0000303|PubMed:19423640"
FT                   /id="VSP_054992"
SQ   SEQUENCE   278 AA;  31450 MW;  70BB23FA9DC18B04 CRC64;
     MSSRSSRTIY VGNLPGDIRE REVEDLFSKY GPVVQIDLKI PPRPPGYAFV EFEDARDADD
     AIYGRDGYDF DGHHLRVELA HGGRRSSHDA RGSYSGRGRG GRGGGDGGGR ERGPSRRSEY
     RVVVSGLPSS ASWQDLKDHM RKGGEVCFSQ VFRDGRGTTG IVDYTSYEDM KYALDDTEFR
     NAFSHEYVRV REYDSRRDSR SPSRGRSYSK SRSRGRSPSR SRSRSRSRSK SRSPKAKSLR
     RSPAKSTSRS PRSRSRSKSR SLSPRGWVTV ERHWIALI
 
 
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